Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a ...
212-498
9.78e-170
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a hexameric nucleoprotein complex (comprising TRF1, TRF2, TIN2, RAP1, POT1 and TPP1 in humans) that protects telomeres, the physical ends of chromosomes. Shelterin protects against these ends being recognized as double-stranded DNA breaks, as well as against degradation of the telomeric overhang by endonucleases. It also helps control access of telomerase to the telomeric overhang, thereby affecting telomore length. This C-terminal region has an OB-fold domain and a holiday junction resolvase (HJR) domain which make dimer contacts with TPP1.
:
Pssm-ID: 380669 Cd Length: 286 Bit Score: 479.86 E-value: 9.78e-170
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
30-147
1.40e-51
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of telomeres 1 protein (hPOT1). POT1 proteins bind to the single-stranded (ss) 3-prime ends of the telomere. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. hPOT1 is implicated in telomere length regulation.
:
Pssm-ID: 239944 Cd Length: 123 Bit Score: 171.06 E-value: 1.40e-51
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a ...
212-498
9.78e-170
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a hexameric nucleoprotein complex (comprising TRF1, TRF2, TIN2, RAP1, POT1 and TPP1 in humans) that protects telomeres, the physical ends of chromosomes. Shelterin protects against these ends being recognized as double-stranded DNA breaks, as well as against degradation of the telomeric overhang by endonucleases. It also helps control access of telomerase to the telomeric overhang, thereby affecting telomore length. This C-terminal region has an OB-fold domain and a holiday junction resolvase (HJR) domain which make dimer contacts with TPP1.
Pssm-ID: 380669 Cd Length: 286 Bit Score: 479.86 E-value: 9.78e-170
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
30-147
1.40e-51
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of telomeres 1 protein (hPOT1). POT1 proteins bind to the single-stranded (ss) 3-prime ends of the telomere. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. hPOT1 is implicated in telomere length regulation.
Pssm-ID: 239944 Cd Length: 123 Bit Score: 171.06 E-value: 1.40e-51
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
22-167
8.04e-49
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a family of fungal telomere protection protein 1 proteins. POT1PC is able to accommodate heterogeneous ssDNA ligands. Pot1 proteins are the proteins responsible for binding to and protecting the 3' single-stranded DNA (ssDNA) overhang at most eukaryotic telomeres.
Pssm-ID: 435514 Cd Length: 152 Bit Score: 165.14 E-value: 8.04e-49
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a ...
212-498
9.78e-170
Protection Of Telomeres Protein 1 (POT1) C-terminal region; POT1 is part of shelterin, a hexameric nucleoprotein complex (comprising TRF1, TRF2, TIN2, RAP1, POT1 and TPP1 in humans) that protects telomeres, the physical ends of chromosomes. Shelterin protects against these ends being recognized as double-stranded DNA breaks, as well as against degradation of the telomeric overhang by endonucleases. It also helps control access of telomerase to the telomeric overhang, thereby affecting telomore length. This C-terminal region has an OB-fold domain and a holiday junction resolvase (HJR) domain which make dimer contacts with TPP1.
Pssm-ID: 380669 Cd Length: 286 Bit Score: 479.86 E-value: 9.78e-170
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of ...
30-147
1.40e-51
hPOT1_OB2: A subfamily of OB folds similar to the second OB fold (OB2) of human protection of telomeres 1 protein (hPOT1). POT1 proteins bind to the single-stranded (ss) 3-prime ends of the telomere. hPOT1 binds specifically to ss telomeric DNA repeats ending with the sequence GGTTAG. The hPOT1 monomer consists of two closely connected OB folds (OB1-OB2) which cooperate to bind telomeric ssDNA. OB1 makes more extensive contact with the ssDNA than OB2. OB2 protects the 3' end of the ssDNA. hPOT1 is implicated in telomere length regulation.
Pssm-ID: 239944 Cd Length: 123 Bit Score: 171.06 E-value: 1.40e-51
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a ...
22-167
8.04e-49
ssDNA-binding domain of telomere protection protein; POT1PC is the ssDNA-binding domain on a family of fungal telomere protection protein 1 proteins. POT1PC is able to accommodate heterogeneous ssDNA ligands. Pot1 proteins are the proteins responsible for binding to and protecting the 3' single-stranded DNA (ssDNA) overhang at most eukaryotic telomeres.
Pssm-ID: 435514 Cd Length: 152 Bit Score: 165.14 E-value: 8.04e-49
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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